Interaction of bovine estrogen receptor with immobilized zinc.
The metal-binding properties of partially purified untransformed or salt-dissociated bovine estrogen receptors were studied using zinc-chelated iminodiacetic acid gels. Only the salt-dissociated 5S receptor is retained by the metal-chelated resin, and this interaction is dependent on the presence of dithiothreitol. The untransformed 9S receptor is not retained, indicating that the zinc-interacting amino acid residues may be masked by receptor-associated proteins such as 90K heat-shock protein or because of an unfavorable receptor conformation.
Atkinson
H C
HC
Department of Obstetrics and Gynaecology, University of Western Australia, King Edward Memorial Hospital for Women, Subiaco.
Ratajczak
T
T
Hähnel
R
R
D000818:Animals; D002417:Cattle; D002614:Chelating Agents; D002846:Chromatography, Affinity; D003600:Cytosol / Q000737:chemistry; D004229:Dithiothreitol; D005782:Gels; D006493:Heparin; D007098:Imino Acids; D011960:Receptors, Estrogen / Q000737:chemistry*; D012588:Scintillation Counting; D012685:Sepharose; D014461:Ultracentrifugation; D015032:Zinc / Q000737:chemistry*
D002614:Chelating Agents; D005782:Gels; D007098:Imino Acids; D011960:Receptors, Estrogen; D006493:Heparin; D012685:Sepharose; D015032:Zinc; D004229:Dithiothreitol; C008109:iminodiacetic acid